KLRI1_RAT
ID KLRI1_RAT Reviewed; 243 AA.
AC Q5DT39; E9PTP0;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Killer cell lectin-like receptor subfamily I member 1 {ECO:0000303|PubMed:15650876};
GN Name=Klri1 {ECO:0000303|PubMed:15650876};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000312|EMBL:AAQ20111.1};
RN [1] {ECO:0000312|EMBL:AAQ20111.1}
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Fischer 344 {ECO:0000312|EMBL:AAQ20111.1};
RX PubMed=15650876; DOI=10.1007/s00251-004-0759-x;
RA Saether P.C., Westgaard I.H., Flornes L.M., Hoelsbrekken S.E., Ryan J.C.,
RA Fossum S., Dissen E.;
RT "Molecular cloning of KLRI1 and KLRI2, a novel pair of lectin-like natural
RT killer-cell receptors with opposing signalling motifs.";
RL Immunogenetics 56:833-839(2005).
RN [2] {ECO:0000312|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3] {ECO:0000305}
RP FUNCTION, SUBUNIT, INTERACTION WITH /KLRE1 AND PTPN6, AND SUBCELLULAR
RP LOCATION.
RX PubMed=18713988; DOI=10.4049/jimmunol.181.5.3177;
RA Saether P.C., Westgaard I.H., Hoelsbrekken S.E., Benjamin J., Lanier L.L.,
RA Fossum S., Dissen E.;
RT "KLRE/I1 and KLRE/I2: a novel pair of heterodimeric receptors that
RT inversely regulate NK cell cytotoxicity.";
RL J. Immunol. 181:3177-3182(2008).
CC -!- FUNCTION: Lectin-like receptor for natural killer (NK) cells.
CC Heterodimer formation with KLRE1 mediates inhibition of NK cell
CC cytolytic activity. {ECO:0000269|PubMed:18713988}.
CC -!- SUBUNIT: Heterodimer with KLRE1. Interacts with PTPN6.
CC {ECO:0000269|PubMed:18713988}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15650876};
CC Single-pass type II membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in natural killer (NK) cells.
CC {ECO:0000269|PubMed:15650876}.
CC -!- DOMAIN: Contains 2 copies of a cytoplasmic motif that is referred to as
CC the immunoreceptor tyrosine-based inhibitor motif (ITIM). The
CC phosphorylated ITIM motif can bind the SH2 domain of several SH2-
CC containing phosphatases leading to down-regulation of cell activation.
CC {ECO:0000250|UniProtKB:P27812}.
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DR EMBL; AY286494; AAQ20111.1; -; mRNA.
DR EMBL; AC108288; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001012667.1; NM_001012649.1.
DR AlphaFoldDB; Q5DT39; -.
DR SMR; Q5DT39; -.
DR STRING; 10116.ENSRNOP00000062814; -.
DR GlyGen; Q5DT39; 5 sites.
DR PaxDb; Q5DT39; -.
DR Ensembl; ENSRNOT00000090813; ENSRNOP00000069881; ENSRNOG00000052803.
DR GeneID; 503651; -.
DR KEGG; rno:503651; -.
DR UCSC; RGD:1359344; rat.
DR CTD; 503550; -.
DR RGD; 1359344; Klri1.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000164228; -.
DR HOGENOM; CLU_049894_9_2_1; -.
DR InParanoid; Q5DT39; -.
DR OMA; CAKLNSH; -.
DR OrthoDB; 1105684at2759; -.
DR PhylomeDB; Q5DT39; -.
DR TreeFam; TF336674; -.
DR PRO; PR:Q5DT39; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000052803; Expressed in spleen and 14 other tissues.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; IBA:GO_Central.
DR GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; IBA:GO_Central.
DR CDD; cd03593; CLECT_NK_receptors_like; 1.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR033992; NKR-like_CTLD.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Glycoprotein; Lectin; Membrane; Receptor;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..243
FT /note="Killer cell lectin-like receptor subfamily I member
FT 1"
FT /id="PRO_0000442200"
FT TOPO_DOM 1..80
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 81..101
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 102..243
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT DOMAIN 137..239
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT MOTIF 16..21
FT /note="ITIM motif 1"
FT /evidence="ECO:0000250|UniProtKB:P27812"
FT MOTIF 47..52
FT /note="ITIM motif 2"
FT /evidence="ECO:0000250|UniProtKB:P27812"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 158..238
FT /evidence="ECO:0000250|UniProtKB:Q13241"
FT DISULFID 217..230
FT /evidence="ECO:0000250|UniProtKB:Q13241"
SQ SEQUENCE 243 AA; 28175 MW; 62BDC48BD0475F94 CRC64;
MPHSKHRDYT ADKQDIPYTE LKACKSPWKH RTPAVKQSPV VLSEEQLKYA ELTFHRTPQL
QPRKQTVRRK RQGPKSAVWR VVTCVLGVLC VVLMITMGIL VPKLFSGQEE QYRETSLHHL
LKNDSSCDPC SHDWIAFGNN FYLFFRGTKS WAESKSACEE LNSHLLDIDS KAELENLLLF
EINGWILVKK NQTNWSSSEN ETKLQHTLID EKKNHSCRYL RGSQFIADDC SSKKPYACEF
NKM
